The active conformation of allophycocyanin from Spirulina platensis studied with spectroscopic analysis.
The active conformation of allophycocyanin from Spirulina platensis studied with spectroscopic analysis.
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通过光谱分析研究钝顶螺旋藻中别藻蓝蛋白的活性构象。
DOI：
10.3964/j.issn.1000-0593(2010)06-1643-04
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发表时间：
2010-06
期刊：
影响因子：
--
通讯作者：
Shao Si-Mi
中科院分区：
文献类型：
--
作者：
Zhang Yu-Zhong;Zhang Xi-Ying;Zhou Bai-Cheng;Peng Guo-Hong;Su Hai-Nan;Shao Si-Mi
采用羟基磷灰石层析和离子交换层析从钝顶螺旋藻中分离纯化别藻蓝蛋白（APC）。研究了溶液pH值对APC光谱的影响。APC在650 nm处具有最大吸收，在620 nm处具有肩峰。荧光发射峰位于660 nm处。吸收光谱和荧光光谱分别反映了APC的能量吸收效率和能量转移效率。APC的结构变化可以通过圆二色光谱监测。APC在不同的pH下显示出良好的吸光度和荧光稳定性，在pH 4-10之间只有微小的变化。APC的三聚体结构得以保持，而蛋白肽的局部变化是允许的，以响应环境干扰。在此pH范围外，APC的二级结构和整体构象发生了显著变化，能量吸收和传递能力也受到了破坏。
Allophycocyanin (APC) was purified from Spirulina platensis using hydroxylapatite chromatography and ion-exchange chromatography. Effects of solution pH on spectra of APC were studied. APC has an absorption maximum at 650 nm, and a shoulder at 620 nm. The fluorescence emission peak is at 660 nm. The efficiency of energy absorbing and transfer in APC could be reflected by the absorption spectra and fluorescence spectra, respectively. Structural variations of APC could be monitored by means of circular dichroism spectra. APC showed good absorbance and fluorescence stability at varying pH with only minor changes between pH 4-10. The trimeric structure of APC was maintained while local variations of protein peptides were allowed in response to the environmental disturbance. Beyond this pH range, secondary structure as well as overall conformation of APC dramatically changed, and the energy absorption and transfer ability were also disrupted.